Enamel proteins are a complex mixture of proteins which probably play a central role in the process of amelogenesis, and the determination of the number of proteins, their structure and sequence of appearance and disappearance during enamel formation is essential to an understanding of that process. With presently available techniques, the proteins solubilized from enamel matrix can be separated into 15 to 25 components. It is not known whether each of these components represents a single protein, the product of an individual gene, or whether the components are interrelated. Possibly, the multiple components are derived from the breakdown of a limited number of proteins either as part of a physiologic process or during the extraction procedures used to isolate the proteins. The overall objective of this proposal is to characterize the enamel proteins and their genes and to attempt to define their role in amelogenesis. Monoclonal antibodies to bovine enamel proteins will be prepared and used to define the immunologic and structural relationships between the proteins. These antibodies will also be used to determine the time of appearance and disappearance of individual proteins during amelogenesis and to localize the proteins in situ by immuno histologic and ultrastructural techniques.